Cell wall proteins of Aquaspirillum serpens.
The Triton X-100-insoluble wall fraction of Aquaspirillum serpens VHA contained three major proteins: the regularly structured (RS) superficial protein (molecular weight 140,000) and two peptidoglycan-associated proteins (molecular weights, 32,000 and 33,000). The molecular arrangement and interactions of the outer membrane and RS proteins were examined with the use of bifunctional cross-linking reagents. The peptidoglycan-associated and RS proteins were not readily cross-linked in either homo- or heteropolymers. This suggests that the free amino groups are not suitably disposed for cross-linking. Some high-molecular-weight multimers of the RS protein were produced, but the subunit structure of the RS array was not stabilized by cross-linking. The peptidoglycan-associated proteins were cross-linked to high-molecular-weight multimers, but no dimers or trimers were produced. This result suggests that these proteins exist in the outer membrane as multimers larger than trimers.
D001419:Bacteria / Q000032:analysis* / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000032:analysis*; D002473:Cell Wall / Q000032:analysis* / Q000187:drug effects; D003432:Cross-Linking Reagents / Q000494:pharmacology; D017830:Octoxynol; D011092:Polyethylene Glycols / Q000494:pharmacology
D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D011092:Polyethylene Glycols; D017830:Octoxynol